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Database: UniProt
Entry: A0A0U3NRZ8_9LACT
LinkDB: A0A0U3NRZ8_9LACT
Original site: A0A0U3NRZ8_9LACT 
ID   A0A0U3NRZ8_9LACT        Unreviewed;       238 AA.
AC   A0A0U3NRZ8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_00074};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00074};
DE   AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
DE            Short=16S rRNA m7G methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074};
GN   Name=rsmG {ECO:0000256|HAMAP-Rule:MF_00074};
GN   ORFNames=NY10_1734 {ECO:0000313|EMBL:ALV22332.1};
OS   Carnobacterium sp. CP1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1564681 {ECO:0000313|EMBL:ALV22332.1, ECO:0000313|Proteomes:UP000064734};
RN   [1] {ECO:0000313|EMBL:ALV22332.1, ECO:0000313|Proteomes:UP000064734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP1 {ECO:0000313|EMBL:ALV22332.1,
RC   ECO:0000313|Proteomes:UP000064734};
RA   Chen J., Yang J., Zhu S., Zhang D., Xiong S.;
RT   "Whole genome Sequence of Carnobacterium sp. strain CP1 Isolated from
RT   Amanda bay, East Antarctic.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the N7 position of a guanine in 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC       methyltransferase RsmG family. {ECO:0000256|HAMAP-Rule:MF_00074}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00074}.
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DR   EMBL; CP010796; ALV22332.1; -; Genomic_DNA.
DR   RefSeq; WP_058919553.1; NZ_CP010796.1.
DR   AlphaFoldDB; A0A0U3NRZ8; -.
DR   STRING; 1564681.NY10_1734; -.
DR   KEGG; carc:NY10_1734; -.
DR   PATRIC; fig|1564681.3.peg.1738; -.
DR   OrthoDB; 9808773at2; -.
DR   Proteomes; UP000064734; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR   InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00138; rsmG_gidB; 1.
DR   PANTHER; PTHR31760; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   PANTHER; PTHR31760:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF02527; GidB; 1.
DR   PIRSF; PIRSF003078; GidB; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00074};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074,
KW   ECO:0000313|EMBL:ALV22332.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064734};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_00074}; S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00074};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00074, ECO:0000313|EMBL:ALV22332.1}.
FT   REGION          218..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         83
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         129..130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         148
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   238 AA;  27091 MW;  8AAADD66D1FC2CA7 CRC64;
     MNPEEFKKAL HDKGIDVTEK QMQQFDHYLV LLQEWNEKIN LTAITEQEEV YLKHFYDSIT
     AGLYVDFNKG VQSLCDVGAG AGFPSIPLKI IFPQLEVTIV DSLNKRIQFL TTLAEKLELE
     GVHFYHDRAE TFGQNKQFRE SFDFVTARAV ARMSVLAELC LPLVKKGGVF IALKASNSDE
     EMKEGQKALA TLGGKFREEF VFELPKEAGE RHVLLIDKKK ETPKKYPRKP GTPNKNPL
//
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